1OBR
CARBOXYPEPTIDASE T
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | OTHER |
| Temperature [K] | 297 |
| Detector technology | FILM |
| Collection date | 1987 |
| Detector | FILM |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 159.420, 159.420, 106.860 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 7.000 - 2.300 |
| Rwork | 0.152 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | CARBOXYPEPTIDASE A (PDB ENTRY 5CPA) |
| RMSD bond length | 0.014 |
| RMSD bond angle | 0.025 |
| Data reduction software | MOSFLM |
| Phasing software | BLANC |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| Rmerge | 0.065 |
| Number of reflections | 21053 |
| Completeness [%] | 61.0 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 | pH 6.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | drop | zinc sulphate | 1 (mM) | |
| 3 | 1 | drop | MPD | 3 (%) | |
| 4 | 1 | drop | ammonium sulfate | 35 (%) | |
| 5 | 1 | drop | MES/NaOH | 50 (mM) |
